RPFC_MYCTU
ID RPFC_MYCTU Reviewed; 176 AA.
AC O07747; L0TAP5;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Resuscitation-promoting factor RpfC;
DE EC=3.-.-.-;
DE Flags: Precursor;
GN Name=rpfC; OrderedLocusNames=Rv1884c; ORFNames=MTCY180.34;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12410821; DOI=10.1046/j.1365-2958.2002.03184.x;
RA Mukamolova G.V., Turapov O.A., Young D.I., Kaprelyants A.S., Kell D.B.,
RA Young M.;
RT "A family of autocrine growth factors in Mycobacterium tuberculosis.";
RL Mol. Microbiol. 46:623-635(2002).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15375142; DOI=10.1128/jb.186.19.6605-6616.2004;
RA Raman S., Hazra R., Dascher C.C., Husson R.N.;
RT "Transcription regulation by the Mycobacterium tuberculosis alternative
RT sigma factor SigD and its role in virulence.";
RL J. Bacteriol. 186:6605-6616(2004).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15207486; DOI=10.1016/j.tube.2003.12.004;
RA Downing K.J., Betts J.C., Young D.I., McAdam R.A., Kelly F., Young M.,
RA Mizrahi V.;
RT "Global expression profiling of strains harbouring null mutations reveals
RT that the five rpf-like genes of Mycobacterium tuberculosis show functional
RT redundancy.";
RL Tuberculosis 84:167-179(2004).
RN [5]
RP MUTAGENESIS OF GLU-80.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15723078; DOI=10.1038/nsmb905;
RA Cohen-Gonsaud M., Barthe P., Bagneris C., Henderson B., Ward J.,
RA Roumestand C., Keep N.H.;
RT "The structure of a resuscitation-promoting factor domain from
RT Mycobacterium tuberculosis shows homology to lysozymes.";
RL Nat. Struct. Mol. Biol. 12:270-273(2005).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18186793; DOI=10.1111/j.1365-2958.2007.06078.x;
RA Kana B.D., Gordhan B.G., Downing K.J., Sung N., Vostroktunova G.,
RA Machowski E.E., Tsenova L., Young M., Kaprelyants A., Kaplan G.,
RA Mizrahi V.;
RT "The resuscitation-promoting factors of Mycobacterium tuberculosis are
RT required for virulence and resuscitation from dormancy but are collectively
RT dispensable for growth in vitro.";
RL Mol. Microbiol. 67:672-684(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Factor that stimulates resuscitation of dormant cells. Has
CC peptidoglycan (PG) hydrolytic activity. Active in the pM concentration
CC range. Has little to no effect on actively-growing cells. PG fragments
CC could either directly activate the resuscitation pathway of dormant
CC bacteria or serve as a substrate for endogenous Rpf, resulting in low
CC molecular weight products with resuscitation activity.
CC {ECO:0000269|PubMed:12410821}.
CC -!- FUNCTION: Stimulates growth of stationary phase M.bovis (a slow-growing
CC Mycobacterium), reduces the lag phase of diluted fast-growers
CC M.smegmatis and Micrococcus luteus. Sequential gene disruption
CC indicates RpfB and RpfE are higher than RpfD and RpfC in functional
CC hierarchy. {ECO:0000269|PubMed:12410821}.
CC -!- INDUCTION: Expressed in actively growing cells, positively regulated by
CC alternative sigma factor SigD, probably directly.
CC {ECO:0000269|PubMed:12410821, ECO:0000269|PubMed:15375142}.
CC -!- DISRUPTION PHENOTYPE: Not essential, disruption of rpfC alone has no
CC effect on growth or survival in liquid culture, nor in mouse infection
CC models, although colony size is reduced. Alterations in gene expression
CC are seen. All 5 genes in this family can be deleted without affecting
CC growth in culture, however triple deletion mutants (rpfA-rpfC-rpfB or
CC rpfA-rpfC-rpfD) are not able to resuscitate spontaneously in the
CC presence or absence of O(2), and are attenuated in a mouse infection
CC model. {ECO:0000269|PubMed:15207486, ECO:0000269|PubMed:18186793}.
CC -!- SIMILARITY: Belongs to the transglycosylase family. Rpf subfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44650.1; -; Genomic_DNA.
DR PIR; A70516; A70516.
DR RefSeq; NP_216400.1; NC_000962.3.
DR RefSeq; WP_003409420.1; NZ_NVQJ01000013.1.
DR PDB; 2N5Z; NMR; -; A=68-146.
DR PDB; 4OW1; X-ray; 1.90 A; A/B/E/S/T/U/W/X=68-159.
DR PDBsum; 2N5Z; -.
DR PDBsum; 4OW1; -.
DR AlphaFoldDB; O07747; -.
DR SMR; O07747; -.
DR STRING; 83332.Rv1884c; -.
DR PaxDb; O07747; -.
DR DNASU; 885759; -.
DR GeneID; 885759; -.
DR KEGG; mtu:Rv1884c; -.
DR PATRIC; fig|83332.111.peg.2094; -.
DR TubercuList; Rv1884c; -.
DR eggNOG; COG1652; Bacteria.
DR InParanoid; O07747; -.
DR OMA; WEEYGGV; -.
DR PhylomeDB; O07747; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:MTBBASE.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MTBBASE.
DR GO; GO:0040010; P:positive regulation of growth rate; IDA:MTBBASE.
DR CDD; cd13925; RPF; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR010618; RPF.
DR Pfam; PF06737; Transglycosylas; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome; Signal; Virulence.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..176
FT /note="Resuscitation-promoting factor RpfC"
FT /id="PRO_0000421029"
FT MUTAGEN 80
FT /note="E->A: Loss of resuscitating activity on M.luteus."
FT /evidence="ECO:0000269|PubMed:15723078"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:4OW1"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4OW1"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:4OW1"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:4OW1"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:2N5Z"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4OW1"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:4OW1"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4OW1"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:4OW1"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:4OW1"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:4OW1"
SQ SEQUENCE 176 AA; 18047 MW; F0FC07A003A781CD CRC64;
MHPLPADHGR SRCNRHPISP LSLIGNASAT SGDMSSMTRI AKPLIKSAMA AGLVTASMSL
STAVAHAGPS PNWDAVAQCE SGGNWAANTG NGKYGGLQFK PATWAAFGGV GNPAAASREQ
QIAVANRVLA EQGLDAWPTC GAASGLPIAL WSKPAQGIKQ IINEIIWAGI QASIPR
